Abstract
Members of the eukaryotic Cdc25 phosphatase family are key targets of the Chk1 and Chk2 checkpoint kinases, which inactivate Cdc25 to halt cell cycle progression when DNA is damaged or incompletely replicated. Now, new kinases that phosphorylate and inactivate Cdc25 are being discovered, including MAPKAP kinase-2, a component of the p38 stress-activated MAP kinase pathway. The roles of other kinases, such as cyclin-dependent kinase, Polo and Aurora A kinase, in controlling the localization or the activation of Cdc25, are controversial. Here, we discuss new data that suggests that different Cdc25 isoforms and regulators of Cdc25 are differentially required for normal cell cycle progression and recovery from checkpoint arrest.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Animals
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Calcium-Calmodulin-Dependent Protein Kinases / metabolism
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Cell Cycle / physiology*
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Cell Cycle Proteins / physiology
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Checkpoint Kinase 2
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DNA Damage
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Humans
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Intracellular Signaling Peptides and Proteins
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Models, Genetic
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Protein Serine-Threonine Kinases / metabolism
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Protein Serine-Threonine Kinases / physiology*
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Schizosaccharomyces pombe Proteins / physiology
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Spindle Apparatus / physiology
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cdc25 Phosphatases / physiology*
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p38 Mitogen-Activated Protein Kinases / metabolism
Substances
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Cell Cycle Proteins
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Intracellular Signaling Peptides and Proteins
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Schizosaccharomyces pombe Proteins
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MAP-kinase-activated kinase 2
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Checkpoint Kinase 2
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CHEK2 protein, human
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Cds1 protein, S pombe
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Plo1 protein, S pombe
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Protein Serine-Threonine Kinases
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Calcium-Calmodulin-Dependent Protein Kinases
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p38 Mitogen-Activated Protein Kinases
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cdc25 Phosphatases